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  1. Article ; Online: Modulation of procaspase-7 self-activation by PEST amino acid residues of the N-terminal prodomain and intersubunit linker.

    Alves, Juliano / Garay-Malpartida, Miguel / Occhiucci, João M / Belizário, José E

    Biochemistry and cell biology = Biochimie et biologie cellulaire

    2017  , Page(s) 1–10

    Abstract: Procaspase-7 zymogen polypeptide is composed of a short prodomain, a large subunit (p20), and a small subunit (p10) connected to an intersubunit linker. Caspase-7 is activated by an initiator caspase-8 and -9, or by autocatalysis after specific cleavage ... ...

    Abstract Procaspase-7 zymogen polypeptide is composed of a short prodomain, a large subunit (p20), and a small subunit (p10) connected to an intersubunit linker. Caspase-7 is activated by an initiator caspase-8 and -9, or by autocatalysis after specific cleavage at IQAD
    Language English
    Publishing date 2017-06-28
    Publishing country Canada
    Document type Journal Article
    ZDB-ID 54104-7
    ISSN 1208-6002 ; 0829-8211
    ISSN (online) 1208-6002
    ISSN 0829-8211
    DOI 10.1139/bcb-2016-0220
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: TAF15 and the leukemia-associated fusion protein TAF15-CIZ/NMP4 are cleaved by caspases-3 and -7.

    Alves, Juliano / Wurdak, Heiko / Garay-Malpartida, Humberto M / Harris, Jennifer L / Occhiucci, João M / Belizário, José E / Li, Jun

    Biochemical and biophysical research communications

    2009  Volume 384, Issue 4, Page(s) 495–500

    Abstract: Caspases are central players in proteolytic pathways that regulate cellular processes such as apoptosis and differentiation. To accelerate the discovery of novel caspase substrates we developed a method combining in silico screening and in vitro ... ...

    Abstract Caspases are central players in proteolytic pathways that regulate cellular processes such as apoptosis and differentiation. To accelerate the discovery of novel caspase substrates we developed a method combining in silico screening and in vitro validation. With this approach, we identified TAF15 as a novel caspase substrate in a trial study. We find that TAF15 was specifically cleaved by caspases-3 and -7. Site-directed mutagenesis revealed the consensus sequence 106DQPD/Y110 as the only site recognized by these caspases. Surprisingly, TAF15 was cleaved at more than one site in staurosporine-treated Jurkat cells. In addition, we generated two oncogenic TAF15-CIZ/NMP4-fused proteins which have been found in acute myeloid leukemia and demonstrate that caspases-3 and -7 cleave the fusion proteins at one single site. Broad application of this combination approach should expedite identification of novel caspase-interacting proteins and provide new insights into the regulation of caspase pathways leading to cell death in normal and cancer cells.
    MeSH term(s) Apoptosis ; Caspase 3/metabolism ; Humans ; Jurkat Cells ; Leukemia, Myeloid, Acute/metabolism ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; TATA-Binding Protein Associated Factors/genetics ; TATA-Binding Protein Associated Factors/metabolism ; Trans-Activators/genetics ; Trans-Activators/metabolism
    Chemical Substances Oncogene Proteins, Fusion ; Recombinant Fusion Proteins ; TAF15 protein, human ; TATA-Binding Protein Associated Factors ; Trans-Activators ; ZNF384 protein, human ; Caspase 3 (EC 3.4.22.-)
    Language English
    Publishing date 2009-07-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2009.05.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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